Herbert Holz

TL;DR: The purification of enzymatically active MSL complexes from Drosophila embryos, Schneider cells, and human HeLa cells reveals an unexpected physical and functional connection between nuclear pore components and chromatin regulation through MSL proteins, highlighting the role of nucleoporins in gene regulation in higher eukaryotes.

TL;DR: The biochemical characterization of the nonspecific lethal (NSL) complex that associates with the histone acetyltransferase MOF in both Drosophila and mammals concludes that the NSL complex acts as a major transcriptional regulator in Drosophile.

TL;DR: This work proposes that Msl1 acts as a scaffold for MSL complex assembly to achieve specific targeting to the X chromosome in Drosophila and shows analogous interactions of MOF with NSL1.

TL;DR: It is proposed that regulated acetylation of MSL-3 may provide a mechanistic explanation for spreading of the dosage compensation complex along the male X chromosome.

TL;DR: The MOF chromobarrel domain directly interacts with nucleic acids and potentiates MOF's enzymatic activity after chromatin binding, making it a unique example of a chromo-like domain directly controlling acetylation activity in vivo.